ArticleProtein science : a publication of the Protein Society1996
Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 79 citations in OpenAlex.
- Article
- Characterisation of three novel α-L-arabinofuranosidases from a compost metagenome.BMC biotechnology · 2019Article
- Extremely stable indole-3-glycerol-phosphate synthase from hyperthermophilic archaeon Pyrococcus furiosus.Extremophiles : life under extreme conditions · 2019Article
- Structural and functional insights into thermally stable cytochrome c' from a thermophile.Protein science : a publication of the Protein Society · 2017Article
- Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Activity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures.Extremophiles : life under extreme conditions · 2016Article
- Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29.Extremophiles : life under extreme conditions · 2015Article
- Prediction of the maximum temperature for life based on the stability of metabolites to decomposition in water.Life (Basel, Switzerland) · 2015Article
- A system for multilocus chromosomal integration and transformation-free selection marker rescue.FEMS yeast research · 2014Article
- Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins.The Journal of biological chemistry · 2011Article
- Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- An irreversible and kinetically controlled process: thermal induced denaturation of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus.The protein journal · 2007Article
- Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity.EMBO reports · 2005Article
- Thermotoga neapolitana adenylate kinase is highly active at 30 degrees C.The Biochemical journal · 2003Article
- Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.Microbiology and molecular biology reviews : MMBR · 2001Review
- Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.Protein science : a publication of the Protein Society · 1999Article
- Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.Nature structural biology · 1997Article
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6 authors at 1 institution in 1 country.
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Abstract
The metabolism of hyperthermophilic microorganisms can function properly at temperatures close to 100 degrees C. It follows that they are equipped with both thermostable enzymes and mechanisms that handle labile metabolites. We wanted to understand how stable and active phosphoribosyl anthranilate isomerase (tPRAI) from the hyperthermophile Thermotoga maritima is at its optimum growth temperature of 80 degrees C, and how its thermolabile substrate, N-(5'-phosphoribosyl)-anthranilate (PRA), is protected from rapid decomposition. To this end, the trpF gene of T. maritima was expressed heterologously in Escherichia coli and tPRAI was purified. In contrast to most PRAIs from mesophiles, which are monomers with the eightfold beta alpha (or TIM) barrel fold, tPRAI is a homodimer. It is strongly resistant toward inactivation by temperatures up to 95 degrees C, by acidification to pH 3.2, and by proteases in the presence and absence of detergents. tPRAI is about 35-fold more active at its physiologic temperature than is the enzyme from E. coli (ePRAI) at 37 degrees C. This high catalytic efficiency of tPRAI is likely to complete successfully with the rapid spontaneous hydrolysis of PRA at 80 degrees C. Thus, with respect to both stability and function, tPRAI appears well adapted to the extreme habitat of T. maritima. Single crystals of tPRAI have been obtained that are suitable for X-ray analysis at high resolution.
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